SitesBLAST
Comparing WP_003946421.1 NCBI__GCF_002893965.1:WP_003946421.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
48% identity, 98% coverage: 10:475/476 of query aligns to 7:474/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
48% identity, 98% coverage: 10:475/476 of query aligns to 7:474/474 of 1wndA
- active site: N149 (= N153), K172 (= K176), E246 (= E249), C280 (= C283), E378 (= E379), D455 (= D456)
- binding calcium ion: G249 (= G252), K250 (= K253), A251 (= A254), G405 (= G406), L406 (= L407), A407 (= A408), Y427 (≠ F428)
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
48% identity, 98% coverage: 10:475/476 of query aligns to 7:474/474 of 1wnbB
- active site: N149 (= N153), K172 (= K176), E246 (= E249), C280 (= C283), E378 (= E379), D455 (= D456)
- binding betaine aldehyde: D279 (= D282), F436 (≠ I437), L438 (= L439)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ V149), A146 (≠ T150), W148 (= W152), K172 (= K176), G204 (= G208), G208 (= G211), D209 (≠ A212), T223 (= T226), G224 (= G227), S225 (= S228), T228 (≠ A231), H231 (≠ A234), G248 (= G251), E378 (= E379)
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
48% identity, 98% coverage: 10:475/476 of query aligns to 7:474/474 of 1wnbA
- active site: N149 (= N153), K172 (= K176), E246 (= E249), C280 (= C283), E378 (= E379), D455 (= D456)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ V149), A146 (≠ T150), W148 (= W152), K172 (= K176), G204 (= G208), G208 (= G211), D209 (≠ A212), G224 (= G227), S225 (= S228), T228 (≠ A231), H231 (≠ A234), G248 (= G251), F380 (= F381)
4f3xA Crystal structure of putative aldehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD
45% identity, 95% coverage: 25:475/476 of query aligns to 22:475/476 of 4f3xA
- active site: N150 (= N153), K173 (= K176), E247 (= E249), C281 (= C283), E379 (= E379), D456 (= D456)
- binding nicotinamide-adenine-dinucleotide: I146 (≠ V149), A147 (≠ T150), P148 (= P151), W149 (= W152), K173 (= K176), E176 (≠ D179), G205 (= G208), G209 (= G211), I213 (≠ V215), I223 (= I225), G225 (= G227), D226 (≠ S228), T229 (≠ A231), G249 (= G251), C281 (= C283), Q328 (≠ H330), R331 (≠ K337), E379 (= E379), F381 (= F381)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
39% identity, 98% coverage: 9:476/476 of query aligns to 7:480/489 of 4o6rA
- active site: N150 (= N153), K173 (= K176), E248 (= E249), C282 (= C283), E383 (= E379), E460 (≠ D456)
- binding adenosine monophosphate: I146 (≠ V149), V147 (≠ T150), K173 (= K176), G206 (= G208), G210 (= G211), Q211 (≠ A212), F224 (≠ I225), G226 (= G227), S227 (= S228), T230 (≠ A231), R233 (≠ A234)
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
39% identity, 97% coverage: 9:471/476 of query aligns to 11:482/497 of P17202
- I28 (= I26) binding K(+)
- D96 (≠ N92) binding K(+)
- SPW 156:158 (≠ TPW 150:152) binding NAD(+)
- Y160 (= Y154) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W161) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPSD 176:179) binding NAD(+)
- L186 (≠ T180) binding K(+)
- SSAT 236:239 (≠ SVRA 228:231) binding NAD(+)
- V251 (≠ L243) binding in other chain
- L258 (= L250) binding NAD(+)
- W285 (≠ F277) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E379) binding NAD(+)
- A441 (= A430) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ L439) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ H445) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K449) binding K(+)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
41% identity, 97% coverage: 9:471/476 of query aligns to 11:485/503 of Q8VWZ1
- N27 (≠ L25) binding Na(+)
- I28 (= I26) binding Na(+)
- D99 (≠ N92) binding Na(+)
- L189 (≠ T180) binding Na(+)
- 238:245 (vs. 227:234, 38% identical) binding NAD(+)
- C294 (= C283) binding NAD(+)
- E393 (= E379) binding NAD(+)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
41% identity, 97% coverage: 9:471/476 of query aligns to 6:480/497 of 3iwkH
- active site: N157 (= N153), K180 (= K176), E255 (= E249), C289 (= C283), E388 (= E379), E465 (≠ D456)
- binding nicotinamide-adenine-dinucleotide: W156 (= W152), G213 (= G208), G217 (= G211), A218 (= A212), G233 (= G227), S234 (= S228), T237 (≠ A231), K240 (≠ A234), C289 (= C283), Q336 (≠ H330), E388 (= E379), F390 (= F381)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
39% identity, 97% coverage: 9:471/476 of query aligns to 9:480/495 of 4v37A